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Structural studies of the binding of malaria surface proteins to human tissue

Research Groupings: Infection and Immunity | Structural and molecular cell biology

Malaria is a major killer in the developing world, affecting half a billion people each year and killing around 2 million. Two of the most deadly forms of the disease are cerebral and placental malaria.

During cerebral malaria, parasite infected red blood cells block tiny blood vessels in the brain, leading to coma, neurological damage and death. In placental malaria, infected red blood cells bind to the placenta causing miscarriage, premature birth and death of mother and child. The interactions at the heart of both of these disease phenotypes involve PfEMP1 proteins, produced by the parasite and displayed on the surface of the infected red blood cell (1). These PfEMP1 proteins interact with human receptors, tethering or clumping the infected erythrocytes and causing the symptoms of disease. Our major goal is to investigate the structures of these PfEMP1 proteins and the molecular basis for their interactions with human receptors.

Previous work includes determination of the crystal structures of components of antibiotic efflux pumps (2), electron microscopic analysis of cyclic nucleotide gated ion channels (3) and electron microscopic studies of clathrin coated pit formation (4). The figure shows the structure of MexA, a component of an antibiotic efflux pump from Pseudomonas aeruginosa (2).

Lab members
Alan Brown, Stephanie Glaser, Pongsak Khunrae, Michael Kucharski

References